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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1980-2-15
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pubmed:abstractText |
The primary structure of two glycopeptides obtained by pronase digestion of chicken ovotransferrin has been investigated by 360-MHz proton nuclear magnetic resonance (NMR) spectroscopy and methylation analysis. The two glycopeptides differ in amino acid composition but contain the same carbohydrate moiety, viz: (formula: see text). Using the NMR data of some reference compounds the chemical shifts of the anomeric protons and mannose H-2 protons could be predicted with an accuracy of 0.01 ppm.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-74
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:574451-Animals,
pubmed-meshheading:574451-Carbohydrate Conformation,
pubmed-meshheading:574451-Carbohydrate Sequence,
pubmed-meshheading:574451-Carbohydrates,
pubmed-meshheading:574451-Chickens,
pubmed-meshheading:574451-Conalbumin,
pubmed-meshheading:574451-Egg Proteins,
pubmed-meshheading:574451-Egg White,
pubmed-meshheading:574451-Glycopeptides,
pubmed-meshheading:574451-Magnetic Resonance Spectroscopy,
pubmed-meshheading:574451-Peptide Fragments
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pubmed:year |
1979
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pubmed:articleTitle |
Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin.
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pubmed:publicationType |
Journal Article
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